2014
DOI: 10.1074/jbc.m114.558536
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Molecular Characterization of Quinate and Shikimate Metabolism in Populus trichocarpa

Abstract: Background: Shikimate is essential for protein biosynthesis. Quinate and its derivatives are protective secondary metabolites. Results: Members of the same gene family encode enzymes with either shikimate or quinate dehydrogenase activity. Conclusion:The molecular genetic basis of plant quinate metabolism has been unraveled in vitro. Significance: Identifying quinate metabolic enzymes will allow testing its ecological function and may enable biotechnological applications.

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Cited by 56 publications
(64 citation statements)
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“…While PoptrQDH2 showed higher specificity towards quinate than shikimate (Guo et al ., ), PintaQDH showed roughly equal specificity towards both compounds. This is consistent with work by Ossipov et al .…”
Section: Discussionmentioning
confidence: 80%
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“…While PoptrQDH2 showed higher specificity towards quinate than shikimate (Guo et al ., ), PintaQDH showed roughly equal specificity towards both compounds. This is consistent with work by Ossipov et al .…”
Section: Discussionmentioning
confidence: 80%
“…Like all SDHs tested here, PintaQDH is dependent on NADP + as a cofactor and showed negligible activities close to the detection limit (not exceeding 0.4 μmol mg −1 min −1 ) when NAD + was used as a cofactor instead for both SDH and QDH activities. Showing the opposite trend, poplar QDHs preferred NAD + to NADP + as a cofactor with either shikimate or quinate as a substrate, as previously described (Guo et al ., ).…”
Section: Resultsmentioning
confidence: 97%
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